REVIEW: Signal Transduction and Protein Phosphorylation in Smooth Muscle Contraction

A. V. Vorotnikov^*, M. A. Krymsky, and V. P. Shirinsky

Laboratory of Cell Motility, Institute of Experimental Cardiology, Cardiology Research Complex, Ministry of Public Health of Russian Federation, 3-ya Cherepkovskaya ul. 15a, Moscow, 121552 Russia; fax: (095) 414-6719; E-mail: A.Vorotnikov@cardio.ru

^* To whom correspondence should be addressed.

Received March 13, 2002; Revision received April 15, 2002

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Smooth muscles are important constituents of vertebrate organisms that provide for contractile activity of internal organs and blood vessels. Basic molecular mechanism of both smooth and striated muscle contractility is the force-producing ATP-dependent interaction of the major contractile proteins, actin and myosin II molecular motor, activated upon elevation of the free intracellular Ca²⁺ concentration ([Ca²⁺]_i). However, whereas striated muscles display a proportionality of generated force to the [Ca²⁺]_i level, smooth muscles feature molecular mechanisms that modulate sensitivity of contractile machinery to [Ca²⁺]_i. Phosphorylation of proteins that regulate functional activity of actomyosin plays an essential role in these modulatory mechanisms. This provides an ability for smooth muscle to contract and maintain tension within a broad range of [Ca²⁺]_i and with a low energy cost, unavailable to a striated muscle. Detailed exploration of these mechanisms is required to understand the molecular organization and functioning of vertebrate contractile systems and for development of novel advances for treating cardiovascular and many other disorders. This review summarizes the currently known and hypothetical mechanisms involved in regulation of smooth muscle Ca²⁺-sensitivity with a special reference to phosphorylation of regulatory proteins of the contractile machinery as a means to modulate their activity.

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KEY WORDS: smooth muscle, Ca²⁺ sensitivity, contraction, phosphorylation, signal transduction, actomyosin regulatory proteins

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